Understanding the Effect of Ionic Liquid on the Folding and Conformation of Small Model Peptides
β Scribed by Huang, Jia Lin; Schmidt, Karson; Murray, Leigh; Noss, Michael E.; Bunagan, Michelle R.
- Book ID
- 122188179
- Publisher
- Biophysical Society
- Year
- 2011
- Tongue
- English
- Weight
- 105 KB
- Volume
- 100
- Category
- Article
- ISSN
- 0006-3495
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## Abstract Melittin is a cationic, amphipathic, hemolytic peptide composed of 26 amino acid residues. It is intrinsically fluorescent due to the presence of a single tryptophan residue, which has been shown to be crucial for its hemolytic activity. It undergoes a structural transition from a rando
Semiempirical AM1 calculations were carried out for quantum-chemically optimized minimum energy conformations of peptides (Ala) 4 -X-(Ala) 4 , where X stands for different L-β£amino acids (Ala,